scholarly journals A New Thermophilic Nitrilase from an Antarctic Hyperthermophilic Microorganism

2016 ◽  
Vol 4 ◽  
Author(s):  
Geraldine V. Dennett ◽  
Jenny M. Blamey
Keyword(s):  
Hyperthermophilic Microorganism

The crystal structure of an esterase from the hyperthermophilic microorganism Pyrobaculum calidifontis VA1 explains its enantioselectivity

2011 ◽  
Vol 91 (4) ◽  
pp. 1061-1072 ◽  
Author(s):  
Gottfried J. Palm ◽  
Elena Fernández-Álvaro ◽  
Xenia Bogdanović ◽  
Sebastian Bartsch ◽  
Jaroslaw Sczodrok ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Pyrobaculum Calidifontis ◽  
Hyperthermophilic Microorganism

Preparation and Characterization of a New Mutant Homolog of the Chemotaxis Protein CheY from the Anaerobic Hyperthermophilic Microorganism Thermotoga Naphthophila

2019 ◽  
Vol 13 (3) ◽  
pp. 244-255
Author(s):  
D. V. Grishin ◽  
Ju. A. Gladilina ◽  
D. D. Zhdanov ◽  
M. V. Pokrovskaya ◽  
I. Yu. Toropygin ◽  
...  
Keyword(s):  
Hyperthermophilic Microorganism

Determination of complete nucleotide sequence of the genome of hyperthermophilic microorganism

2008 ◽  
Vol 421 (1) ◽  
pp. 204-206
Author(s):  
K. G. Skryabin ◽  
A. V. Mardanov ◽  
I. V. Kublanov ◽  
E. A. Bonch-Osmolovskaya ◽  
N. V. Ravin
Keyword(s):  
Nucleotide Sequence ◽  
Complete Nucleotide Sequence ◽  
Hyperthermophilic Microorganism

scholarly journals Metal cation binding by the hyperthermophilic microorganism, Archaea Methanocaldococcus Jannaschii, and its effects on silicification

Palaeontology ◽  
2011 ◽  
Vol 54 (5) ◽  
pp. 953-964 ◽  
Author(s):  
FRANÇOIS ORANGE ◽  
JEAN-ROBERT DISNAR ◽  
FRANCES WESTALL ◽  
DANIEL PRIEUR ◽  
PATRICK BAILLIF
Keyword(s):  
Metal Cation ◽  
Cation Binding ◽  
Methanocaldococcus Jannaschii ◽  
Hyperthermophilic Microorganism

scholarly journals Preparation and characterization of a new mutant homolog of chemotaxis protein CheY from anaerobic hyperthermophilic microorganism Thermotoga naphthophila

2019 ◽  
Vol 65 (1) ◽  
pp. 41-50
Author(s):  
D.V. Grishin ◽  
Ju.A. Gladilina ◽  
D.D. Zhdanov ◽  
M.V. Pokrovskaya ◽  
I.Yu. Toropygin ◽  
...  
Keyword(s):  
Recombinant Proteins ◽  
Bacterial Chemotaxis ◽  
Laboratory Strain ◽  
Expression Vectors ◽  
Cultivation Conditions ◽  
Kinetics Parameters ◽  
E Coli ◽  
Hyperthermophilic Microorganism ◽  
The Impact

Using genetic engineering methods the expression vectors structures have been designed to produce recombinant proteins TnaCheY and Tna CheY-mut, the homologues of the chemotaxis protein CheY from the hyperthermophilic organism Thermotoga naphthophila in Escherichia coli BL21(DE3) cells. The cultivation conditions of transformed strains were optimized. The influence of episomal expression of the heterologous chemotaxis protein CheY on growth kinetics parameters of the culture of mesophilic bacteria E. coli was studied. The optimal purification flowchart of the obtained proteins using thermolysis is proposed. Using the E. coli BL21(DE3) laboratory strain as an example, the possibility of employment the episomal expression of such proteins to control the cultivation and production time of pharmaceutically and industrially valuable metabolites due to the impact on some stages of the bacterial chemotaxis is experimentally proved.

Glycolipids from Thermotoga maritima, a hyperthermophilic microorganism belonging to Bacteria domain

1992 ◽  
Vol 1124 (3) ◽  
pp. 249-252 ◽  
Author(s):  
M.Cristina Manca ◽  
Barbara Nicolaus ◽  
Virginia Lanzotti ◽  
Antonio Trincone ◽  
Agata Gambacorta ◽  
...  
Keyword(s):  
Thermotoga Maritima ◽  
Hyperthermophilic Microorganism

scholarly journals Xyloglucan Oligosaccharides Hydrolysis by Exo-Acting Glycoside Hydrolases from Hyperthermophilic Microorganism Saccharolobus solfataricus

2021 ◽  
Vol 22 (7) ◽  
pp. 3325
Author(s):  
Nicola Curci ◽  
Andrea Strazzulli ◽  
Roberta Iacono ◽  
Federica De De Lise ◽  
Luisa Maurelli ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Industrial Applications ◽  
Apple Pomace ◽  
Glycoside Hydrolases ◽  
Hyperthermophilic Archaea ◽  
Industrial Processes ◽  
Degrading Enzymes ◽  
Hyperthermophilic Microorganism ◽  
Hydrolysis Of ◽  
Harsh Conditions

In the field of biocatalysis and the development of a bio-based economy, hemicellulases have attracted great interest for various applications in industrial processes. However, the study of the catalytic activity of the lignocellulose-degrading enzymes needs to be improved to achieve the efficient hydrolysis of plant biomasses. In this framework, hemicellulases from hyperthermophilic archaea show interesting features as biocatalysts and provide many advantages in industrial applications thanks to their stability in the harsh conditions encountered during the pretreatment process. However, the hemicellulases from archaea are less studied compared to their bacterial counterpart, and the activity of most of them has been barely tested on natural substrates. Here, we investigated the hydrolysis of xyloglucan oligosaccharides from two different plants by using, both synergistically and individually, three glycoside hydrolases from Saccharolobus solfataricus: a GH1 β-gluco-/β-galactosidase, a α-fucosidase belonging to GH29, and a α-xylosidase from GH31. The results showed that the three enzymes were able to release monosaccharides from xyloglucan oligosaccharides after incubation at 65 °C. The concerted actions of β-gluco-/β-galactosidase and the α-xylosidase on both xyloglucan oligosaccharides have been observed, while the α-fucosidase was capable of releasing all α-linked fucose units from xyloglucan from apple pomace, representing the first GH29 enzyme belonging to subfamily A that is active on xyloglucan.

Sign in / Sign up

Export Citation Format

Share Document